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Protein

Vacuolar protein sorting-associated protein 26B

Gene

VPS26B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. May be involved in retrograde transport of SORT1 but not of IGF2R. Acts redundantly with VSP26A in SNX-27 mediated endocytic recycling of SLC2A1/GLUT1 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Vacuolar protein sorting-associated protein 26B
Alternative name(s):
Vesicle protein sorting 26B
Gene namesi
Name:VPS26B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:28119. VPS26B.

Subcellular locationi

  • Cytoplasm By similarity
  • Membrane; Peripheral membrane protein By similarity
  • Early endosome By similarity
  • Late endosome By similarity

  • Note: Localizes to early and late endosomal structures (By similarity).By similarity

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • early endosome Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • late endosome Source: UniProtKB
  • retromer complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endosome, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394747.

Polymorphism and mutation databases

BioMutaiVPS26B.
DMDMi110816482.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 336336Vacuolar protein sorting-associated protein 26BPRO_0000247089Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei302 – 3021Phosphoserine2 Publications
Modified residuei304 – 3041Phosphoserine2 Publications
Modified residuei319 – 3191Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ4G0F5.
PaxDbiQ4G0F5.
PeptideAtlasiQ4G0F5.
PRIDEiQ4G0F5.

PTM databases

PhosphoSiteiQ4G0F5.

Expressioni

Gene expression databases

BgeeiQ4G0F5.
CleanExiHS_VPS26B.
ExpressionAtlasiQ4G0F5. baseline and differential.
GenevisibleiQ4G0F5. HS.

Organism-specific databases

HPAiHPA038172.

Interactioni

Subunit structurei

Component of the heterotrimeric retromer cargo-selective complex (CSC), also described as vacuolar protein sorting VPS subcomplex (VPS,) formed by VPS26 (VPS26A or VPS26B), VPS29 and VPS35. The CSC has a highly elongated structure with VPS26 and VPS29 binding independently at opposite distal ends of VPS35 as central platform. The CSC is believed to associate with variable sorting nexins to form functionally distinct retromer complex variants. The originally described retromer complex (also called SNX-BAR retromer) is a pentamer containing the CSC and a heterodimeric membrane-deforming subcomplex formed between SNX1 or SNX2 and SNX5 or SNX6 (also called SNX-BAR subcomplex); the respective CSC and SNX-BAR subcomplexes associate with low affinity. The CSC associates with SNX3 to form a SNX3-retromer complex. The CSC associates with SNX27, the WASH complex and the SNX-BAR subcomplex to form the SNX27-retromer complex. Interacts with VPS29, VPS35, TBC1D5, GOLPH3, SNX27 (By similarity).By similarity

Protein-protein interaction databases

BioGridi125215. 15 interactions.
IntActiQ4G0F5. 1 interaction.
STRINGi9606.ENSP00000281187.

Structurei

3D structure databases

ProteinModelPortaliQ4G0F5.
SMRiQ4G0F5. Positions 9-296.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the VPS26 family.Curated

Phylogenomic databases

eggNOGiNOG256244.
GeneTreeiENSGT00390000002588.
HOGENOMiHOG000191799.
HOVERGENiHBG082914.
InParanoidiQ4G0F5.
KOiK18466.
OMAiFFSFGQS.
OrthoDBiEOG7NW699.
PhylomeDBiQ4G0F5.
TreeFamiTF300907.

Family and domain databases

InterProiIPR028934. Vps26-related.
[Graphical view]
PfamiPF03643. Vps26. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4G0F5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSFFGFGQSV EVEILLNDAE SRKRAEHKTE DGKKEKYFLF YDGETVSGKV
60 70 80 90 100
SLALKNPNKR LEHQGIKIEF IGQIELYYDR GNHHEFVSLV KDLARPGEIT
110 120 130 140 150
QSQAFDFEFT HVEKPYESYT GQNVKLRYFL RATISRRLND VVKEMDIVVH
160 170 180 190 200
TLSTYPELNS SIKMEVGIED CLHIEFEYNK SKYHLKDVIV GKIYFLLVRI
210 220 230 240 250
KIKHMEIDII KRETTGTGPN VYHENDTIAK YEIMDGAPVR GESIPIRLFL
260 270 280 290 300
AGYELTPTMR DINKKFSVRY YLNLVLIDEE ERRYFKQQEV VLWRKGDIVR
310 320 330
KSMSHQAAIA SQRFEGTTSL GEVRTPSQLS DNNCRQ
Length:336
Mass (Da):39,155
Last modified:July 25, 2006 - v2
Checksum:i1C07D0ABA7797A12
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti55 – 551K → R in AAH98386 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF452718 mRNA. Translation: AAP13353.1.
BC009747 mRNA. Translation: AAH09747.1.
BC014128 mRNA. Translation: AAH14128.1.
BC098386 mRNA. Translation: AAH98386.1.
CCDSiCCDS8495.1.
RefSeqiNP_443107.1. NM_052875.4.
UniGeneiHs.334684.

Genome annotation databases

EnsembliENST00000281187; ENSP00000281187; ENSG00000151502.
ENST00000525095; ENSP00000434162; ENSG00000151502.
GeneIDi112936.
KEGGihsa:112936.
UCSCiuc001qhe.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF452718 mRNA. Translation: AAP13353.1.
BC009747 mRNA. Translation: AAH09747.1.
BC014128 mRNA. Translation: AAH14128.1.
BC098386 mRNA. Translation: AAH98386.1.
CCDSiCCDS8495.1.
RefSeqiNP_443107.1. NM_052875.4.
UniGeneiHs.334684.

3D structure databases

ProteinModelPortaliQ4G0F5.
SMRiQ4G0F5. Positions 9-296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi125215. 15 interactions.
IntActiQ4G0F5. 1 interaction.
STRINGi9606.ENSP00000281187.

PTM databases

PhosphoSiteiQ4G0F5.

Polymorphism and mutation databases

BioMutaiVPS26B.
DMDMi110816482.

Proteomic databases

MaxQBiQ4G0F5.
PaxDbiQ4G0F5.
PeptideAtlasiQ4G0F5.
PRIDEiQ4G0F5.

Protocols and materials databases

DNASUi112936.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000281187; ENSP00000281187; ENSG00000151502.
ENST00000525095; ENSP00000434162; ENSG00000151502.
GeneIDi112936.
KEGGihsa:112936.
UCSCiuc001qhe.3. human.

Organism-specific databases

CTDi112936.
GeneCardsiGC11P134094.
HGNCiHGNC:28119. VPS26B.
HPAiHPA038172.
MIMi610027. gene.
neXtProtiNX_Q4G0F5.
PharmGKBiPA128394747.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG256244.
GeneTreeiENSGT00390000002588.
HOGENOMiHOG000191799.
HOVERGENiHBG082914.
InParanoidiQ4G0F5.
KOiK18466.
OMAiFFSFGQS.
OrthoDBiEOG7NW699.
PhylomeDBiQ4G0F5.
TreeFamiTF300907.

Miscellaneous databases

ChiTaRSiVPS26B. human.
GeneWikiiVPS26B.
GenomeRNAii112936.
NextBioi78701.
PROiQ4G0F5.
SOURCEiSearch...

Gene expression databases

BgeeiQ4G0F5.
CleanExiHS_VPS26B.
ExpressionAtlasiQ4G0F5. baseline and differential.
GenevisibleiQ4G0F5. HS.

Family and domain databases

InterProiIPR028934. Vps26-related.
[Graphical view]
PfamiPF03643. Vps26. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Kim N.-S., Shon H.-Y., Oh J.-H., Lee J.-Y., Kim J.-M., Hahn Y., Park H.-S., Kim S., Kim Y.S.
    Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye, Lung and Placenta.
  3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  4. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  6. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302 AND SER-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiVP26B_HUMAN
AccessioniPrimary (citable) accession number: Q4G0F5
Secondary accession number(s): Q96A55
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: July 22, 2015
This is version 89 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 11
    Human chromosome 11: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.